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2h32
From Proteopedia
(New page: 200px<br /> <applet load="2h32" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h32, resolution 2.70Å" /> '''Crystal structure o...) |
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| - | [[Image:2h32. | + | [[Image:2h32.jpg|left|200px]]<br /><applet load="2h32" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2h32" size=" | + | |
caption="2h32, resolution 2.70Å" /> | caption="2h32, resolution 2.70Å" /> | ||
'''Crystal structure of the pre-B cell receptor'''<br /> | '''Crystal structure of the pre-B cell receptor'''<br /> | ||
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==Overview== | ==Overview== | ||
The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell, development. In the 2.7 angstrom structure of a human pre-BCR Fab-like, fragment, consisting of an antibody heavy chain (HC) paired with the, surrogate light chain, the "unique regions" of VpreB and lambda5 replace, the complementarity-determining region 3 (CDR3) loop of an antibody light, chain and appear to "probe" the HC CDR3, potentially influencing the, selection of the antibody repertoire. Biochemical analysis indicates that, the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling, mechanism. | The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell, development. In the 2.7 angstrom structure of a human pre-BCR Fab-like, fragment, consisting of an antibody heavy chain (HC) paired with the, surrogate light chain, the "unique regions" of VpreB and lambda5 replace, the complementarity-determining region 3 (CDR3) loop of an antibody light, chain and appear to "probe" the HC CDR3, potentially influencing the, selection of the antibody repertoire. Biochemical analysis indicates that, the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling, mechanism. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Agammaglobulinemia, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146770 146770]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2H32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2H32 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H32 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: v and c-type ig folds]] | [[Category: v and c-type ig folds]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:34:47 2008'' |
Revision as of 13:34, 23 January 2008
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Crystal structure of the pre-B cell receptor
Overview
The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell, development. In the 2.7 angstrom structure of a human pre-BCR Fab-like, fragment, consisting of an antibody heavy chain (HC) paired with the, surrogate light chain, the "unique regions" of VpreB and lambda5 replace, the complementarity-determining region 3 (CDR3) loop of an antibody light, chain and appear to "probe" the HC CDR3, potentially influencing the, selection of the antibody repertoire. Biochemical analysis indicates that, the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling, mechanism.
About this Structure
2H32 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insight into pre-B cell receptor function., Bankovich AJ, Raunser S, Juo ZS, Walz T, Davis MM, Garcia KC, Science. 2007 Apr 13;316(5822):291-4. PMID:17431183
Page seeded by OCA on Wed Jan 23 15:34:47 2008
